Heath, GR, Li, M, Rong, H et al. (5 more authors) (2017) Multilayered lipid membrane stacks for biocatalysis using membrane enzymes. Advanced Functional Materials, 27 (17). 1606265. ISSN 1616-301X
Abstract
Multilayered or stacked lipid membranes are a common principle in biology and have various functional advantages compared to single lipid membranes, such as their ability to spatially organize processes, compartmentalize molecules and greatly increase surface area and hence membrane protein concentration. Here we report on a supramolecular assembly of a multilayered lipid membrane system in which poly-L-lysine electrostatically links negatively charged lipid membranes. When suitable membrane enzymes are incorporated, either an ubiquinol oxidase (cytochrome bo3 from Escherichia coli) or an oxygen tolerant hydrogenase (the membrane-bound hydrogenase from Ralstonia eutropha), cyclic voltammetry (CV) reveals a linear increase in biocatalytic activity with each additional membrane layer. Electron transfer between the enzymes and the electrode is mediated by the quinone pool that is present in the lipid phase. We deduce by atomic force microscopy, CV and fluorescence microscopy that quinones are able to diffuse between the stacked lipid membrane layers via defect sites where the lipid membranes are interconnected. This assembly is akin to that of interconnected thylakoid membranes or the folded lamella of mitochondria and have significant potential for mimicry in biotechnology applications such as energy production or biosensing.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2017 The Authors. Published by WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. The copyright line of this paper was changed 5 April 2017 after initial publication. |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Biomedical Sciences (Leeds) |
Funding Information: | Funder Grant number BBSRC BB/L020130/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 21 Feb 2017 09:56 |
Last Modified: | 21 Oct 2017 19:26 |
Published Version: | https://doi.org/10.1002/adfm.201606265 |
Status: | Published |
Publisher: | Wiley |
Identification Number: | 10.1002/adfm.201606265 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:112590 |